| Literature DB >> 33169665 |
Joseph Shaw1,2, Rajendra Gosain2,3, Monoj Mon Kalita4, Toshana L Foster1,2, Jayakanth Kankanala2,3, D Ram Mahato4, Sonia Abas2,3, Barnabas J King5, Claire Scott1,2, Emma Brown1,2, Matthew J Bentham1,2, Laura Wetherill1,2, Abigail Bloy1,2, Adel Samson1, Mark Harris2,6, Jamel Mankouri2,6, David J Rowlands2,6, Andrew Macdonald2,6, Alexander W Tarr5, Wolfgang B Fischer4, Richard Foster2,3, Stephen Griffin1,2.
Abstract
Since the 1960s, a single class of agent has been licensed targeting virus-encoded ion channels, or 'viroporins', contrasting the success of channel blocking drugs in other areas of medicine. Although resistance arose to these prototypic adamantane inhibitors of the influenza A virus (IAV) M2 proton channel, a growing number of clinically and economically important viruses are now recognised to encode essential viroporins providing potential targets for modern drug discovery. We describe the first rationally designed viroporin inhibitor with a comprehensive structure-activity relationship (SAR). This step-change in understanding not only revealed a second biological function for the p7 viroporin from hepatitis C virus (HCV) during virus entry, but also enabled the synthesis of a labelled tool compound that retained biological activity. Hence, p7 inhibitors (p7i) represent a unique class of HCV antiviral targeting both the spread and establishment of infection, as well as a precedent for future viroporin-targeted drug discovery.Entities:
Keywords: antiviral drugs; biochemistry; chemical biology; hepatitis c virus; human; infectious disease; microbiology; p7; virion egress; viroporin; virus; virus entry
Year: 2020 PMID: 33169665 PMCID: PMC7714397 DOI: 10.7554/eLife.52555
Source DB: PubMed Journal: Elife ISSN: 2050-084X Impact factor: 8.140